ABCC7 p.Glu267Ala
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PMID: 23478129
[PubMed]
Billet A et al: "CFTR: effect of ICL2 and ICL4 amino acids in close spatial proximity on the current properties of the channel."
No.
Sentence
Comment
72
In order to change the properties of the side chains, we replaced each amino acid by a small, uncharged residue (mutants E267A-CFTR and K1060A-CFTR) or by an oppositely charged residue (mutants E267R-CFTR, K1060E-CFTR).
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ABCC7 p.Glu267Ala 23478129:72:121
status: NEW86 100 200 -50 50 100 -100 100 100 100 200 C D B A I (pA/pF) I (pA/pF) I (pA/pF) V (mV) V (mV) V (mV) 5000pA 50ms E267R-K1060E E267A E267R K1060A K1060E E267A E267R wt E267R-K1060E K1060A K1060E ICL4 ICL2 K1060 E267 ICL1 ICL3 K1060 E267 ICL4 ICL2 ICL1 ICL3 % of maturation B C wt E267A E267R K1060A K1060E E267R-K1060E wt -50 50 100 -100 100 200 -50 50 100 -100 100 Fig. 2.
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ABCC7 p.Glu267Ala 23478129:86:124
status: NEWX
ABCC7 p.Glu267Ala 23478129:86:150
status: NEWX
ABCC7 p.Glu267Ala 23478129:86:277
status: NEW93 Dotted lines represent a maturation similar to that of the wt protein (C, D) Whole cell chloride currents of HEK293 cells expressing wt-CFTR, E267A/R-, K1060A/Eor E267R-K1060E-CFTR mutants in presence of 10 bc;M Fsk.
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ABCC7 p.Glu267Ala 23478129:93:142
status: NEW105 First, the presence of a small and uncharged residue at the E267 position (E267A mutant) decreased by approximately 50% the Cl-current density compared to wt.
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ABCC7 p.Glu267Ala 23478129:105:75
status: NEW107 For K1060, irrespective of the replacement of the positively charged side chain by a small uncharged residue (K1060A mutant) or a negatively charged residue (K1060E mutant), the inward and outward Cl-current densities were 50-60% lower than the corresponding Cl-currents elicited by wt channels but similar to that of the E267A mutant.
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ABCC7 p.Glu267Ala 23478129:107:322
status: NEW137 We observed that the abolition of one charged residue in the E267A or K1060A mutants induced a 50% diminution of the Cl-current density (Fig. 2).
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ABCC7 p.Glu267Ala 23478129:137:61
status: NEW
PMID: 25190805
[PubMed]
Wang W et al: "An electrostatic interaction at the tetrahelix bundle promotes phosphorylation-dependent cystic fibrosis transmembrane conductance regulator (CFTR) channel opening."
No.
Sentence
Comment
256
These authors observed greater inhibition by a charge-reversal mutation than by a neutral substitution at the E267 position (E267R versus E267A), as we showed here in our more detailed mechanistic study.
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ABCC7 p.Glu267Ala 25190805:256:138
status: NEW